ID   SUCA_RAT                Reviewed;         346 AA.
AC   P13086; Q6P7S4;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03222};
DE            EC=6.2.1.4 {ECO:0000255|HAMAP-Rule:MF_03222};
DE            EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_03222};
DE   AltName: Full=Succinyl-CoA synthetase subunit alpha {ECO:0000255|HAMAP-Rule:MF_03222};
DE            Short=SCS-alpha {ECO:0000255|HAMAP-Rule:MF_03222};
DE   Flags: Precursor;
GN   Name=Suclg1 {ECO:0000255|HAMAP-Rule:MF_03222};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-346.
RC   TISSUE=Liver;
RX   PubMed=3422742; DOI=10.1073/pnas.85.5.1432;
RA   Henning W.D., Upton C., McFadden G., Majumdar R., Bridger W.A.;
RT   "Cloning and sequencing of the cytoplasmic precursor to the alpha subunit
RT   of rat liver mitochondrial succinyl-CoA synthetase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:1432-1436(1988).
CC   -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle
CC       (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of
CC       either ATP or GTP and thus represents the only step of substrate-level
CC       phosphorylation in the TCA. The alpha subunit of the enzyme binds the
CC       substrates coenzyme A and phosphate, while succinate binding and
CC       specificity for either ATP or GTP is provided by different beta
CC       subunits. {ECO:0000255|HAMAP-Rule:MF_03222}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + succinate = ADP + phosphate + succinyl-CoA;
CC         Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC         ChEBI:CHEBI:456216; EC=6.2.1.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03222};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA + GTP + succinate = GDP + phosphate + succinyl-CoA;
CC         Xref=Rhea:RHEA:22120, ChEBI:CHEBI:30031, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC         ChEBI:CHEBI:58189; EC=6.2.1.4; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03222};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC       from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_03222}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Different beta
CC       subunits determine nucleotide specificity. Together with the ATP-
CC       specific beta subunit SUCLA2, forms an ADP-forming succinyl-CoA
CC       synthetase (A-SCS). Together with the GTP-specific beta subunit SUCLG2
CC       forms a GDP-forming succinyl-CoA synthetase (G-SCS).
CC       {ECO:0000255|HAMAP-Rule:MF_03222}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03222}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_03222}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA41233.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
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DR   EMBL; BC061537; AAH61537.2; -; mRNA.
DR   EMBL; J03621; AAA41233.1; ALT_SEQ; mRNA.
DR   PIR; A28962; SYRTSA.
DR   RefSeq; NP_446204.2; NM_053752.2.
DR   AlphaFoldDB; P13086; -.
DR   SMR; P13086; -.
DR   BioGRID; 250390; 6.
DR   CORUM; P13086; -.
DR   IntAct; P13086; 8.
DR   MINT; P13086; -.
DR   STRING; 10116.ENSRNOP00000007624; -.
DR   iPTMnet; P13086; -.
DR   PhosphoSitePlus; P13086; -.
DR   SwissPalm; P13086; -.
DR   jPOST; P13086; -.
DR   PaxDb; 10116-ENSRNOP00000007624; -.
DR   GeneID; 114597; -.
DR   KEGG; rno:114597; -.
DR   UCSC; RGD:619821; rat.
DR   AGR; RGD:619821; -.
DR   CTD; 8802; -.
DR   RGD; 619821; Suclg1.
DR   eggNOG; KOG1255; Eukaryota.
DR   HOGENOM; CLU_052104_1_0_1; -.
DR   InParanoid; P13086; -.
DR   OrthoDB; 474at2759; -.
DR   PhylomeDB; P13086; -.
DR   TreeFam; TF300666; -.
DR   Reactome; R-RNO-71403; Citric acid cycle (TCA cycle).
DR   UniPathway; UPA00223; UER00999.
DR   PRO; PR:P13086; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:0009361; C:succinate-CoA ligase complex (ADP-forming); IBA:GO_Central.
DR   GO; GO:0045244; C:succinate-CoA ligase complex (GDP-forming); IDA:RGD.
DR   GO; GO:0019003; F:GDP binding; IDA:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IDA:RGD.
DR   GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IDA:RGD.
DR   GO; GO:0006105; P:succinate metabolic process; IDA:RGD.
DR   GO; GO:0006104; P:succinyl-CoA metabolic process; IDA:RGD.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IDA:RGD.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR   HAMAP; MF_01988; Succ_CoA_alpha; 1.
DR   InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR   InterPro; IPR033847; Citrt_syn/SCS-alpha_CS.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR005810; CoA_lig_alpha.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR005811; SUCC_ACL_C.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   NCBIfam; TIGR01019; sucCoAalpha; 1.
DR   PANTHER; PTHR11117:SF2; SUCCINATE--COA LIGASE [ADP_GDP-FORMING] SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11117; SUCCINYL-COA LIGASE SUBUNIT ALPHA; 1.
DR   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PIRSF; PIRSF001553; SucCS_alpha; 1.
DR   PRINTS; PR01798; SCOASYNTHASE.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
DR   PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR   PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
DR   Genevisible; P13086; RN.
PE   2: Evidence at transcript level;
KW   Acetylation; Ligase; Mitochondrion; Nucleotide-binding; Reference proteome;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..34
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT   CHAIN           35..346
FT                   /note="Succinate--CoA ligase [ADP/GDP-forming] subunit
FT                   alpha, mitochondrial"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT                   /id="PRO_0000033343"
FT   ACT_SITE        299
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222,
FT                   ECO:0000269|PubMed:3422742"
FT   BINDING         64..67
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT   BINDING         90
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT   BINDING         143..145
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared with subunit beta"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT   MOD_RES         54
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P53597"
FT   MOD_RES         57
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT   MOD_RES         57
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT   MOD_RES         66
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT   MOD_RES         66
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT   MOD_RES         81
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT   MOD_RES         94
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT   MOD_RES         105
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT   MOD_RES         338
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT   CONFLICT        153
FT                   /note="V -> L (in Ref. 2; AAA41233)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   346 AA;  36148 MW;  2DDFC746C11B5B0C CRC64;
     MTAAVVAAAA TATMVSGSSG LAAARLLSRT FLLQQNGIRH GSYTASRKNI YIDKNTKVIC
     QGFTGKQGTF HSQQALEYGT KLVGGTTPGK GGKKHLGLPV FNTVKEAKEK TGATASVIYV
     PPPFAAAAIN EAIDAEIPLV VCITEGIPQQ DMVRVKHKLT RQGKTRLIGP NCPGIINPGE
     CKIGIMPGHI HKKGRIGIVS RSGTLTYEAV HQTTQVGLGQ SLCIGIGGDP FNGTNFIDCL
     DVFLKDPATE GIVLIGEIGG HAEENAAEFL KEHNSGPKAK PVVSFIAGIT APPGRRMGHA
     GAIIAGGKGG AKEKISALQS AGVIVSMSPA QLGTCMYKEF EKRKML
//